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Reviewed, UniProtKB/Swiss-Prot Q9Y7B1 (ACOX_PICPA)

Last modified January 19, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A oxidase
      Short name=Acyl-CoA oxidase
    EC=1.3.3.6
Gene names
Name: POX1
OrganismPichia pastoris (Yeast)
Taxonomic identifier4922 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

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Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome Ref.1.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

acyl-CoA oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719Acyl-coenzyme A oxidase
PRO_0000204700

Regions

Motif716 – 7194Microbody targeting signal

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Sequences

Sequence LengthMass (Da)Tools
Q9Y7B1-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 252DC1E03BD978F0

FASTA71980,519
        10         20         30         40         50         60 
MFKIESIKSQ SPQVAIDKER KATKFDINKM FEFLESGKDE AALTKSLMQQ IERDTILKTN 

        70         80         90        100        110        120 
ASYYDLTKDQ HRELTAQKIA RLASYIEKDA PFFENFQKRL NLIAIVDPQL GTRVGVHLGL 

       130        140        150        160        170        180 
FLSAIRGNGT EEQFKYWAFE RGAAYLKDVY GCFGMTELAH GSNVAGLETT ATFDQKTKEF 

       190        200        210        220        230        240 
EINTPHLGAT KWWIGGAAHS ANHCVVYARL IVSGKDYGVK TFVVPIRDRN HNLHSGVAIG 

       250        260        270        280        290        300 
DIGAKMGRDG IDNGWIQLTN VRIPMNYMRS KFTKVTQRQE IVEVPPLEQL AYGALLGGRV 

       310        320        330        340        350        360 
TMVTDSFRMA QRFITIALRY SVGRRQFGAK NSSEELKLID YPLHQRRLLP YLALTYALSI 

       370        380        390        400        410        420 
SSFDLSQTYD SVLSNLDAAG KSQDFSKLGQ AIAGLKNLFC ASASLKSTAT WYVAQLIDEC 

       430        440        450        460        470        480 
RQACGGHGYS SYSGFGKAYN DWVVQCTWEG DNNILASNAG RLLCNLLSSC KKKEKKIKGD 

       490        500        510        520        530        540 
LSYLNGISNI DKEAICWNKQ SMTNLSNSNI DKELFCFNKQ VCTVKLINAI QGTIIRLGVR 

       550        560        570        580        590        600 
VPNIGSKKST WDDIAAQRVV LSKLNAVLYM LQHLVLKIKQ LGDEEAHKQY LVQIAALFAT 

       610        620        630        640        650        660 
SQIEMNFASY FLQFKAIDSL EPVADVVSEL CLSVRDQVIG LTDSFQFSDY FINSALGSHS 

       670        680        690        700        710 
GDIYNTYFDT VNNLNNPQVR DGKAAYSEAL EAMLRRDPLE VRECFEKSDK VLKKLAPKI

« Hide

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References

[1]"Analysis of the peroxisomal acyl-CoA oxidase gene product from Pichia pastoris and determination of its targeting signal."
Koller A., Spong A.P., Luers G.H., Subramani S.
Yeast 15:1035-1044(1999) [PubMed: 10455228] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TARGETING SIGNAL.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF133102 Genomic DNA. Translation: AAD31029.1.

3D structure databases

SMRQ9Y7B1. Positions 15-696.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.6. 390.

Family and domain databases

InterProIPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameACOX_PICPA
AccessionPrimary (citable) accession number: Q9Y7B1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1999
Last modified: January 19, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents